ID S0AQM9_FERAC Unreviewed; 354 AA.
AC S0AQM9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00787};
DE EC=2.1.1.195 {ECO:0000256|HAMAP-Rule:MF_00787};
DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000256|HAMAP-Rule:MF_00787};
GN Name=cbiD {ECO:0000256|HAMAP-Rule:MF_00787};
GN ORFNames=FACI_IFERC00001G0365 {ECO:0000313|EMBL:AGO60345.1};
OS Ferroplasma acidarmanus Fer1.
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Ferroplasmaceae; Ferroplasma.
OX NCBI_TaxID=333146 {ECO:0000313|EMBL:AGO60345.1, ECO:0000313|Proteomes:UP000014660};
RN [1] {ECO:0000313|EMBL:AGO60345.1, ECO:0000313|Proteomes:UP000014660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=fer1 {ECO:0000313|Proteomes:UP000014660};
RX PubMed=17267615; DOI=10.1073/pnas.0604851104;
RA Allen E.E., Tyson G.W., Whitaker R.J., Detter J.C., Richardson P.M.,
RA Banfield J.F.;
RT "Genome dynamics in a natural archaeal population.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1883-1888(2007).
CC -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC form cobalt-precorrin-6A. {ECO:0000256|HAMAP-Rule:MF_00787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26285, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:60063, ChEBI:CHEBI:60064;
CC EC=2.1.1.195; Evidence={ECO:0000256|HAMAP-Rule:MF_00787};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 6/10. {ECO:0000256|HAMAP-Rule:MF_00787}.
CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000256|HAMAP-
CC Rule:MF_00787}.
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DR EMBL; CP004145; AGO60345.1; -; Genomic_DNA.
DR RefSeq; WP_009886387.1; NC_021592.1.
DR AlphaFoldDB; S0AQM9; -.
DR GeneID; 16024512; -.
DR KEGG; fac:FACI_IFERC01G0365; -.
DR PATRIC; fig|333146.12.peg.381; -.
DR HOGENOM; CLU_041273_0_0_2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000014660; Chromosome.
DR GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2110.10; CbiD-like; 1.
DR HAMAP; MF_00787; CbiD; 1.
DR InterPro; IPR002748; CbiD.
DR InterPro; IPR036074; CbiD_sf.
DR NCBIfam; TIGR00312; cbiD; 1.
DR PANTHER; PTHR35863; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR35863:SF1; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR Pfam; PF01888; CbiD; 1.
DR PIRSF; PIRSF026782; CbiD; 1.
DR SUPFAM; SSF111342; CbiD-like; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00787}; Reference proteome {ECO:0000313|Proteomes:UP000014660};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00787}.
SQ SEQUENCE 354 AA; 38610 MW; 89D2FA999F651881 CRC64;
MYIENPDRTN LRYGYTTGAC ATAATRAALI MMVTGKTVDY VEINLPAKKT ARFLIENSKI
YENYCIASVK KDGGDDPDVT TGLYIYSRVE YSEKSGIEIT GGEGVGVVTK EGLPIKPGNP
AINPVPLKML RAAATEVLDS YEVHRGLKIT ISVPGGAEVA TKTCNPKLGI IGGISILGTR
GIVIPFSDSS WKASIVLGIR VASRMDMDTL VFSTGGRSDT AVHKIFPDFK EEQFIEIGDF
LGFSVKRAVD TGIRNLVIAG MPGKISKLAD NNMDLHSSKS SVNFDFLASI GKKIGYPDEI
ISRIRHANTV LNVMEIINYD SIFLDTLKER SIENINKITG NKIKVDIEII KNEY
//
